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Principaux documents

C2409

Sigma-Aldrich

Creatinase from microorganisms

lyophilized powder, ≥4 units/mg solid

Synonyme(s) :

Creatine Amidinohydrolase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Actinobacillus spp.)

Niveau de qualité

Forme

lyophilized powder

Activité spécifique

≥4 units/mg solid

Poids mol.

~100 kDa

Température de stockage

−20°C

Description générale

Creatinase is a homodimer that catalyzes hydrolysis of creatine. It consists of two monomer subunits and two defined domains; N and C terminal domains. The C-terminal fold has both the α helices and anti-parallel β sheet within two structurally similar domains.In between these two domains, a sulfhydryl group acts as active site, and the activity is metal-independent.

Application

Creatinase mixed with sarcosine oxidase may be used to determine the level of creatine in different pH, temperature, enzyme ratio, and buffer concentration. It may also be used to determine the plasma creatinine level by using a centrifugal analyser.

Actions biochimiques/physiologiques

Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride.

Propriétés physiques

Isoelectric point: 4.6 ± 0.1
Michaelis constant: 1.9 x 10‾2M (Creatine)
Structure: 2 subunits per mole of enzyme
Inhibitors: Cu++, Hg++, Ag+
Optimum pH: 8.0
Optimum temp: 40°C
pH Stability: pH 5.5 − 9.0 (25°C, 16hr)
Thermal stability: Below 50°C (pH 7.5, 30 min)

Définition de l'unité

One unit will hydrolyze 1.0 μmole of creatine to urea and sarcosine per min at pH 7.5 at 37 °C.

Forme physique

Lyophilized powder containing sugars and EDTA as stabilizers

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Les clients ont également consulté

J F Bazan et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(7), 2473-2477 (1994-03-29)
Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) are related. A detailed comparison of the three-dimensional folds of the two enzymes confirms this
Balasundaram Padmanabhan et al.
Acta crystallographica. Section D, Biological crystallography, 58(Pt 8), 1322-1328 (2002-07-24)
The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4)
H Crocker et al.
Journal of clinical pathology, 41(5), 576-581 (1988-05-01)
An enzymatic kit method for the determination of plasma creatinine was optimised for use with a centrifugal analyser and its performance characteristics and practicability compared with an end point and a kinetic Jaffé-based method. The enzymatic method exhibited several advantages
M-L Lee
Pediatric cardiology, 26(6), 792-796 (2005-08-06)
I report on a 3-month-old infant with pulmonary atresia-intact ventricular septum and ventriculocoronary communication (VCC) who underwent percutaneous radiofrequency valvulotomy and valvuloplasty (RFVV). The patient's cardiac troponin-I, creatine kinase (CK), and myocardial fraction of (CK-MB) were elevated before RFVV and
Ashutosh Tiwari et al.
International journal of biological macromolecules, 44(5), 408-412 (2009-05-12)
A matrix made up of chitosan-SiO(2)-multiwall carbon nanotubes (CHIT-SiO(2)-MWCNTs) nanocomposite was fabricated to investigate the immobilization of creatine amidinohydrolase (CAH). CAH enzyme was covalently immobilized with the CHIT-SiO(2)-MWCNTs matrix using glutaraldehyde as a linker. The resulting CAH/CHIT-SiO(2)-MWCNTs biomatrix was characterized

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